Q4WIF3
Gene name |
cpr6 (AFUA_2G02050) |
Protein name |
Peptidyl-prolyl cis-trans isomerase D |
Names |
PPIase D, Rotamase D |
Species |
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
KEGG Pathway |
afm:AFUA_2G02050 |
EC number |
5.2.1.8: Cis-trans isomerases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q4WIF3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q4WIF3-F1 | Predicted | AlphaFoldDB |
No variants for Q4WIF3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q4WIF3 | |||||
No associated diseases with Q4WIF3
5 regional properties for Q4WIF3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | Tetratricopeptide repeat 1 | 314 - 346 | IPR001440 |
| domain | Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain | 11 - 178 | IPR002130 |
| repeat | Tetratricopeptide repeat | 220 - 253 | IPR019734-1 |
| repeat | Tetratricopeptide repeat | 314 - 347 | IPR019734-2 |
| conserved_site | Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site | 63 - 80 | IPR020892 |
Functions
| Description | ||
|---|---|---|
| EC Number | 5.2.1.8 | Cis-trans isomerases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| intracellular membrane-bounded organelle | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| cyclosporin A binding | Binding to cyclosporin A, a cyclic undecapeptide that contains several N-methylated and unusual amino acids. |
| peptidyl-prolyl cis-trans isomerase activity | Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. |
| protein peptidyl-prolyl isomerization | The modification of a protein by cis-trans isomerization of a proline residue. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAETQRRPRV | YFDIQIGSQK | AGRIALELVR | LPFNDVVPKT | AENFRALCTG | EKGVGKQRKP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LSYKGSIFHR | VIKQFMIQGG | DFTNFNGTGG | ESIYGEKFPD | ENFELKHDRP | FLLSMANSGP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GTNGSQFFIT | TVPTPHLDGK | HVVFGEVING | KSIVRKIENM | PTQADKPTTD | VTIVDCGELS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GEDYENATKQ | VADATGDPYE | DYPDDHQGEE | LNAQVCFKIA | SELKNFGNTA | FKSGDVALGL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DKYQKGLRYL | NEFPDPDEND | PKDLEPQMKS | LRFTLHSNSS | LLANKLGQYK | NAQNWATYAL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EVADAANAKE | ADRAKAYYRR | AVAYSGQKEE | DEALKDLQEA | LKLAPGDAGI | LNEIAKVKKA |
| 370 | |||||
| IKDSEAKEKA | AARKFFS |